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Gel-free proteomic methodologies to study reversible cysteine oxidation and irreversible protein carbonyl formation

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dc.contributor.author Boronat i Llop, Susanna, 1965-
dc.contributor.author García Santamarina, Sarela, 1978-
dc.contributor.author Hidalgo Hernando, Elena
dc.date.accessioned 2016-01-14T15:45:16Z
dc.date.available 2016-03-17T03:00:03Z
dc.date.issued 2015
dc.identifier.citation Boronat S, García-Santamarina S, Hidalgo E. Gel-free proteomic methodologies to study reversible cysteine oxidation and irreversible protein carbonyl formation. Free Radical Research. 2015;49(5):494-510. DOI: 10.3109/10715762.2015.1009053
dc.identifier.issn 1071-5762
dc.identifier.uri http://hdl.handle.net/10230/25578
dc.description.abstract Oxidative modifications in proteins have been traditionally considered as hallmarks of damage by oxidative stress and aging. However, oxidants can generate a huge variety of reversible and irreversible modifications in amino acid side chains as well as in the protein backbones, and these post-translational modifications can contribute to the activation of signal transduction pathways, and also mediate the toxicity of oxidants. Among the reversible modifications, the most relevant ones are those arising from cysteine oxidation. Thus, formation of sulfenic acid or disulfide bonds is known to occur in many enzymes as part of their catalytic cycles, and it also participates in the activation of signaling cascades. Furthermore, these reversible modifications have been usually attributed with a protective role, since they may prevent the formation of irreversible damage by scavenging reactive oxygen species. Among irreversible modifications, protein carbonyl formation has been linked to damage and death, since it cannot be repaired and can lead to protein loss-of-function and to the formation of protein aggregates. This review is aimed at researchers interested on the biological consequences of oxidative stress, both at the level of signaling and toxicity. Here we are providing a concise overview on current mass-spectrometry-based methodologies to detect reversible cysteine oxidation and irreversible protein carbonyl formation in proteomes. We do not pretend to impose any of the different methodologies, but rather to provide an objective catwalk on published gel-free approaches to detect those two types of modifications, from a biologist's point of view.
dc.description.sponsorship This work was supported by the Spanish Ministry of Science and Innovation (BFU2012-32045), PLAN E and FEDER, and by SGR2009-195 from Generalitat de Catalunya (Spain) to E.H. J.A. and E. H. are recipients of ICREA Academia Awards (Generalitat de Catalunya).
dc.format.mimetype application/pdf
dc.language.iso eng
dc.publisher Taylor & Francis (Routledge)
dc.relation.ispartof Free Radical Research. 2015;49(5):494-510
dc.rights © Taylor & Francis. This is an electronic version of an article published in: Boronat S, García-Santamarina S, Hidalgo E. Gel-free proteomic methodologies to study reversible cysteine oxidation and irreversible protein carbonyl formation. Free Radical Research. 2015; 49(5). Free Radical Research is available online at: http://www.tandfonline.com/doi/abs/10.3109/10715762.2015.1009053
dc.subject.other Reacció d'oxidació-reducció
dc.subject.other Proteòmica
dc.title Gel-free proteomic methodologies to study reversible cysteine oxidation and irreversible protein carbonyl formation
dc.type info:eu-repo/semantics/article
dc.identifier.doi http://dx.doi.org/10.3109/10715762.2015.1009053
dc.subject.keyword Cys oxidation
dc.subject.keyword H2O2 reactivity
dc.subject.keyword Protein carbonyl formation
dc.subject.keyword Redox proteomics
dc.subject.keyword Redox regulation
dc.relation.projectID info:eu-repo/grantAgreement/ES/3PN/BFU2012-32045
dc.rights.accessRights info:eu-repo/semantics/openAccess
dc.type.version info:eu-repo/semantics/acceptedVersion

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